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The phosphorylation-specific association of STMN1 with GRP78 promotes breast cancer metastasis

Metastasis is a major cause of death in patients with breast cancer. Stathmin1 (STMN1) is a phosphoprotein associated with cancer metastasis. It exhibits a complicated phosphorylation pattern in response to various extracellular signals, but its signaling mechanism is poorly understood. In this stud... Full description

Journal Title: Cancer Letters 10 July 2016, Vol.377(1), pp.87-96
Main Author: Kuang, Xia-Ying
Other Authors: Jiang, He-Sheng , Li, Kai , Zheng, Yi-Zi , Liu, Yi-Rong , Qiao, Feng , Li, Shan , Hu, Xin , Shao, Zhi-Ming
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0304-3835 ; E-ISSN: 1872-7980 ; DOI: 10.1016/j.canlet.2016.04.035
Link: https://www.sciencedirect.com/science/article/pii/S0304383516302713
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recordid: elsevier_sdoi_10_1016_j_canlet_2016_04_035
title: The phosphorylation-specific association of STMN1 with GRP78 promotes breast cancer metastasis
format: Article
creator:
  • Kuang, Xia-Ying
  • Jiang, He-Sheng
  • Li, Kai
  • Zheng, Yi-Zi
  • Liu, Yi-Rong
  • Qiao, Feng
  • Li, Shan
  • Hu, Xin
  • Shao, Zhi-Ming
subjects:
  • Stathmin
  • Phosphorylation
  • Grp78
  • Breast Cancer
  • Metastasis
  • Medicine
ispartof: Cancer Letters, 10 July 2016, Vol.377(1), pp.87-96
description: Metastasis is a major cause of death in patients with breast cancer. Stathmin1 (STMN1) is a phosphoprotein associated with cancer metastasis. It exhibits a complicated phosphorylation pattern in response to various extracellular signals, but its signaling mechanism is poorly understood. In this study, we report that phosphorylation of STMN1 at Ser25 and Ser38 is necessary to maintain cell migration capabilities and is associated with shorter disease-free survival (DFS) in breast cancer. In addition, we report that glucose-regulated protein of molecular mass 78 (GRP78) is a novel phospho-STMN1 binding protein upon STMN1 Ser25/Ser38 phosphorylation. This phosphorylation-dependent interaction is regulated by MEK kinase and is required for STMN1-GRP78 complex stability and STMN1-mediated migration. We also propose a prognostic model based on phospho-STMN1 and GRP78 to assess metastatic risk in breast cancer patients.
language: eng
source:
identifier: ISSN: 0304-3835 ; E-ISSN: 1872-7980 ; DOI: 10.1016/j.canlet.2016.04.035
fulltext: fulltext
issn:
  • 0304-3835
  • 03043835
  • 1872-7980
  • 18727980
url: Link


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titleThe phosphorylation-specific association of STMN1 with GRP78 promotes breast cancer metastasis
creatorKuang, Xia-Ying ; Jiang, He-Sheng ; Li, Kai ; Zheng, Yi-Zi ; Liu, Yi-Rong ; Qiao, Feng ; Li, Shan ; Hu, Xin ; Shao, Zhi-Ming
ispartofCancer Letters, 10 July 2016, Vol.377(1), pp.87-96
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subjectStathmin ; Phosphorylation ; Grp78 ; Breast Cancer ; Metastasis ; Medicine
descriptionMetastasis is a major cause of death in patients with breast cancer. Stathmin1 (STMN1) is a phosphoprotein associated with cancer metastasis. It exhibits a complicated phosphorylation pattern in response to various extracellular signals, but its signaling mechanism is poorly understood. In this study, we report that phosphorylation of STMN1 at Ser25 and Ser38 is necessary to maintain cell migration capabilities and is associated with shorter disease-free survival (DFS) in breast cancer. In addition, we report that glucose-regulated protein of molecular mass 78 (GRP78) is a novel phospho-STMN1 binding protein upon STMN1 Ser25/Ser38 phosphorylation. This phosphorylation-dependent interaction is regulated by MEK kinase and is required for STMN1-GRP78 complex stability and STMN1-mediated migration. We also propose a prognostic model based on phospho-STMN1 and GRP78 to assess metastatic risk in breast cancer patients.
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titleThe phosphorylation-specific association of STMN1 with GRP78 promotes breast cancer metastasis
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Metastasis is a major cause of death in patients with breast cancer. Stathmin1 (STMN1) is a phosphoprotein associated with cancer metastasis. It exhibits a complicated phosphorylation pattern in response to various extracellular signals, but its signaling mechanism is poorly understood. In this study, we report that phosphorylation of STMN1 at Ser25 and Ser38 is necessary to maintain cell migration capabilities and is associated with shorter disease-free survival (DFS) in breast cancer. In addition, we report that glucose-regulated protein of molecular mass 78 (GRP78) is a novel phospho-STMN1 binding protein upon STMN1 Ser25/Ser38 phosphorylation. This phosphorylation-dependent interaction is regulated by MEK kinase and is required for STMN1-GRP78 complex stability and STMN1-mediated migration. We also propose a prognostic model based on phospho-STMN1 and GRP78 to assess metastatic risk in breast cancer patients.

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Metastasis is a major cause of death in patients with breast cancer. Stathmin1 (STMN1) is a phosphoprotein associated with cancer metastasis. It exhibits a complicated phosphorylation pattern in response to various extracellular signals, but its signaling mechanism is poorly understood. In this study, we report that phosphorylation of STMN1 at Ser25 and Ser38 is necessary to maintain cell migration capabilities and is associated with shorter disease-free survival (DFS) in breast cancer. In addition, we report that glucose-regulated protein of molecular mass 78 (GRP78) is a novel phospho-STMN1 binding protein upon STMN1 Ser25/Ser38 phosphorylation. This phosphorylation-dependent interaction is regulated by MEK kinase and is required for STMN1-GRP78 complex stability and STMN1-mediated migration. We also propose a prognostic model based on phospho-STMN1 and GRP78 to assess metastatic risk in breast cancer patients.

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lad01Cancer Letters
date2016-07-10